Hermione Potter, Wife Of A Legend
by slutpharma
Summary: What if Harry and Hermione were actually soul mates? Reimagining of the first Harry Potter book with Hermione and Harry falling for eachother. M for Lemons.


**ipid-anchored proteins** (also known as **lipid-linked proteins** ) are proteins located on the surface of the cell membrane that are covalently attached to lipids embedded within the cell membrane. These proteins insert and assume a place in the bilayer structure of the membrane alongside the similar fatty acid tails. The lipid-anchored protein can be located on either side of the cell , the lipid serves to anchor the protein to the cell membrane. **ipid-anchored proteins** (also known as **lipid-linked proteins** ) are proteins located on the surface of the cell membrane that are covalently attached to lipids embedded within the cell membrane. These proteins insert and assume a place in the bilayer structure of the membrane alongside the similar fatty acid tails. The lipid-anchored protein can be located on either side of the cell , the lipid serves to anchor the protein to the cell lipid groups play a role in protein interaction and can contribute to the function of the protein to which it is , the lipid serves as a mediator of membrane associations or as a determinant for specific protein-protein interactions.

For example, lipid groups can play an important role in increasing molecular hydrophobicity. This allows for the interaction of proteins with cellular membranes and protein domains.

Overall, there are three main types of lipid-anchored proteins which include **prenylated proteins** , **fatty acylated proteins** and **glycosylphosphatidylinositol-linked proteins (GPI).** A protein can have multiple lipid groups covalently attached to it, but the site where the lipid binds to the protein depends both on the lipid group and protein.

S-palmitoylation (i.e. attachment of palmitic acid) is a reversible protein modification in which a palmitic acid is attached to a specific cysteine residue via thioester linkage. The term S-acylation can also be used when other medium and long fatty acids chains are also attached to palmitoylated proteins. No consensus sequence for protein palmitoylation has been identified. Palmitoylated proteins are mainly found on the cytoplasmic side of the plasma membrane where they play a role in transmembrane signaling. The palmitoyl group can be removed by palmitoyl thioesterases. It is believed that this reverse palmitoylation may regulate the interaction of the protein with the membrane and thus have a role in signaling processes

]Furthermore, this allows for the regulation of protein subcellular localization, stability and trafficking. An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can play a role in the regulation of neurotransmitter release.

 **Glycosylphosphatidylinositols** **(GPI)** proteins are attached to a GPI complex molecular group via an amide linkage to the protein's C-terminal carboxyl group. This GPI complex consists of several main components that are all interconnected: a phosphoethanolamine, a linear tetrasaccharide (composed of three mannose and a glucosaminyl) and a phosphatidylinositol. The phosphatidylinositol group is glycosidically linked to the non-N-acetylated glucosamine of the tetrasaccharide. A phosphodiester bond is then formed between the mannose at the nonreducing end (of the tetrasaccaride) and the phosphoethanolamine. The phosphoethanolamine is then amide linked to the C-terminal of the carboxyl group of the respective protein. The GPI attachment occurs through the action of GPI-transamidase fatty acid chains of the phosphatidylinositol are inserted into the membrane and thus are what anchor the protein to the membrane. These proteins are only located on the exterior surface of the plasma membrane.]

Releasing the IZUMO1R/JUNO GPI protein from the egg plasma membrane does not allow for sperm to fuse with the egg and it is suggested that this mechanism may contribute to the polyspermy block at the plasma membrane in eggs

]Furthermore, this allows for the regulation of protein subcellular localization, stability and trafficking. An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can play a role in the regulation of neurotransmitter release.

Releasing the IZUMO1R/JUNO GPI protein from the egg plasma membrane does not allow for sperm to fuse with the egg and it is suggested that this mechanism may contribute to the polyspermy block at the plasma membrane in eggs

]Furthermore, this allows for the regulation of protein subcellular localization, stability and trafficking. An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can play a role in the regulation of neurotransmitter release.

 **ipid-anchored proteins** (also known as **lipid-linked proteins** ) are proteins located on the surface of the cell membrane that are covalently attached to lipids embedded within the cell membrane. These proteins insert and assume a place in the bilayer structure of the membrane alongside the similar fatty acid tails. The lipid-anchored protein can be located on either side of the cell , the lipid serves to anchor the protein to the cell membrane. **ipid-anchored proteins** (also known as **lipid-linked proteins** ) are proteins located on the surface of the cell membrane that are covalently attached to lipids embedded within the cell membrane. These proteins insert and assume a place in the bilayer structure of the membrane alongside the similar fatty acid tails. The lipid-anchored protein can be located on either side of the cell , the lipid serves to anchor the protein to the cell lipid groups play a role in protein interaction and can contribute to the function of the protein to which it is , the lipid serves as a mediator of membrane associations or as a determinant for specific protein-protein interactions.

For example, lipid groups can play an important role in increasing molecular hydrophobicity. This allows for the interaction of proteins with cellular membranes and protein domains.

Overall, there are three main types of lipid-anchored proteins which include **prenylated proteins** , **fatty acylated proteins** and **glycosylphosphatidylinositol-linked proteins (GPI).** A protein can have multiple lipid groups covalently attached to it, but the site where the lipid binds to the protein depends both on the lipid group and protein.

S-palmitoylation (i.e. attachment of palmitic acid) is a reversible protein modification in which a palmitic acid is attached to a specific cysteine residue via thioester linkage. The term S-acylation can also be used when other medium and long fatty acids chains are also attached to palmitoylated proteins. No consensus sequence for protein palmitoylation has been identified. Palmitoylated proteins are mainly found on the cytoplasmic side of the plasma membrane where they play a role in transmembrane signaling. The palmitoyl group can be removed by palmitoyl thioesterases. It is believed that this reverse palmitoylation may regulate the interaction of the protein with the membrane and thus have a role in signaling processes

]Furthermore, this allows for the regulation of protein subcellular localization, stability and trafficking. An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can play a role in the regulation of neurotransmitter release.

 **Glycosylphosphatidylinositols** **(GPI)** proteins are attached to a GPI complex molecular group via an amide linkage to the protein's C-terminal carboxyl group. This GPI complex consists of several main components that are all interconnected: a phosphoethanolamine, a linear tetrasaccharide (composed of three mannose and a glucosaminyl) and a phosphatidylinositol. The phosphatidylinositol group is glycosidically linked to the non-N-acetylated glucosamine of the tetrasaccharide. A phosphodiester bond is then formed between the mannose at the nonreducing end (of the tetrasaccaride) and the phosphoethanolamine. The phosphoethanolamine is then amide linked to the C-terminal of the carboxyl group of the respective protein. The GPI attachment occurs through the action of GPI-transamidase fatty acid chains of the phosphatidylinositol are inserted into the membrane and thus are what anchor the protein to the membrane. These proteins are only located on the exterior surface of the plasma membrane.]

Releasing the IZUMO1R/JUNO GPI protein from the egg plasma membrane does not allow for sperm to fuse with the egg and it is suggested that this mechanism may contribute to the polyspermy block at the plasma membrane in eggs

]Furthermore, this allows for the regulation of protein subcellular localization, stability and trafficking. An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can play a role in the regulation of neurotransmitter release.

Releasing the IZUMO1R/JUNO GPI protein from the egg plasma membrane does not allow for sperm to fuse with the egg and it is suggested that this mechanism may contribute to the polyspermy block at the plasma membrane in eggs

]Furthermore, this allows for the regulation of protein subcellular localization, stability and trafficking. An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can play a role in the regulation of neurotransmitter release.

 **ipid-anchored proteins** (also known as **lipid-linked proteins** ) are proteins located on the surface of the cell membrane that are covalently attached to lipids embedded within the cell membrane. These proteins insert and assume a place in the bilayer structure of the membrane alongside the similar fatty acid tails. The lipid-anchored protein can be located on either side of the cell , the lipid serves to anchor the protein to the cell membrane. **ipid-anchored proteins** (also known as **lipid-linked proteins** ) are proteins located on the surface of the cell membrane that are covalently attached to lipids embedded within the cell membrane. These proteins insert and assume a place in the bilayer structure of the membrane alongside the similar fatty acid tails. The lipid-anchored protein can be located on either side of the cell , the lipid serves to anchor the protein to the cell lipid groups play a role in protein interaction and can contribute to the function of the protein to which it is , the lipid serves as a mediator of membrane associations or as a determinant for specific protein-protein interactions.

For example, lipid groups can play an important role in increasing molecular hydrophobicity. This allows for the interaction of proteins with cellular membranes and protein domains.

Overall, there are three main types of lipid-anchored proteins which include **prenylated proteins** , **fatty acylated proteins** and **glycosylphosphatidylinositol-linked proteins (GPI).** A protein can have multiple lipid groups covalently attached to it, but the site where the lipid binds to the protein depends both on the lipid group and protein.

S-palmitoylation (i.e. attachment of palmitic acid) is a reversible protein modification in which a palmitic acid is attached to a specific cysteine residue via thioester linkage. The term S-acylation can also be used when other medium and long fatty acids chains are also attached to palmitoylated proteins. No consensus sequence for protein palmitoylation has been identified. Palmitoylated proteins are mainly found on the cytoplasmic side of the plasma membrane where they play a role in transmembrane signaling. The palmitoyl group can be removed by palmitoyl thioesterases. It is believed that this reverse palmitoylation may regulate the interaction of the protein with the membrane and thus have a role in signaling processes

]Furthermore, this allows for the regulation of protein subcellular localization, stability and trafficking. An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can play a role in the regulation of neurotransmitter release.

 **Glycosylphosphatidylinositols** **(GPI)** proteins are attached to a GPI complex molecular group via an amide linkage to the protein's C-terminal carboxyl group. This GPI complex consists of several main components that are all interconnected: a phosphoethanolamine, a linear tetrasaccharide (composed of three mannose and a glucosaminyl) and a phosphatidylinositol. The phosphatidylinositol group is glycosidically linked to the non-N-acetylated glucosamine of the tetrasaccharide. A phosphodiester bond is then formed between the mannose at the nonreducing end (of the tetrasaccaride) and the phosphoethanolamine. The phosphoethanolamine is then amide linked to the C-terminal of the carboxyl group of the respective protein. The GPI attachment occurs through the action of GPI-transamidase fatty acid chains of the phosphatidylinositol are inserted into the membrane and thus are what anchor the protein to the membrane. These proteins are only located on the exterior surface of the plasma membrane.]

Releasing the IZUMO1R/JUNO GPI protein from the egg plasma membrane does not allow for sperm to fuse with the egg and it is suggested that this mechanism may contribute to the polyspermy block at the plasma membrane in eggs

]Furthermore, this allows for the regulation of protein subcellular localization, stability and trafficking. An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can play a role in the regulation of neurotransmitter release.

Releasing the IZUMO1R/JUNO GPI protein from the egg plasma membrane does not allow for sperm to fuse with the egg and it is suggested that this mechanism may contribute to the polyspermy block at the plasma membrane in eggs

]Furthermore, this allows for the regulation of protein subcellular localization, stability and trafficking. An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can play a role in the regulation of neurotransmitter release.


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